Abstract
Peroxidase isozymes are distributed throughout the plant kingdom. In order to understand the functions of the isoperoxidases, the nature and degree of the heterogeneity between them need to be clarified. The cationic (C.PRX) and the anionic peanut peroxidases (A.PRX) are used for such a study.;The physico-chemical properties of the two peroxidases are reported. They are similar in MW, carbohydrate content and pH optimum for catalysis, but differ in Ca{dollar}\\sp{lcub}2+{rcub}{dollar} contents and isoelectric point. The basis for the difference in pI is found in the different relative content of the acidic and basic amino acids, with more acidic residues present in the anionic and more basic ones in the cationic isozyme.;Polyclonal antibodies generated to each isozyme and monoclonal antibodies to the C.PRX were used to probe the antigenic structures of the two peroxidases by double-immunodiffusion, ELISA, immunoinhibition of enzyme activity and Western blotting. The polyclonal antisera reacted not only with the homologous but also with the non-homologous isozyme, suggesting similarities in antigenic structure exist between the two peroxidases. The cross-reaction is partially attributed to the epitopes present in the carbohydrate moieties and near the active sites of the isozymes. On the other hand, the monoclonal antibodies recognized more specifically the C.PRX.;Radiolabeling of peanut cell cultures coupled with immunoprecipitation reveals that four times as much C.PRX is released into the medium as the A.PRX, although no substantial difference was observed in the rate of their synthesis. This release is not prevented by treatment of the cultures with tunicamycin, an inhibitor of N-linked glycosylation. Subcellular localization by immunogold-labeling with their antibodies demonstrates that both peroxidases are associated with Golgi complexes and amyloplasts. The C.PRX is also found on the cell walls while the A.PRX on the plasmalemma.;Evidence obtained from deglycosylation with glycopeptidase F, oxidation of carbohydrates with periodate and inhibition of glycosylation with tunicamycin indicates that the carbohydrate side chains distributed on the surface of the peroxidases are essential for expression of the enzyme activity and for maintenance of the stability of the molecules.
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Claims 15
Claim · model-written summary
The cationic and anionic peanut peroxidases are similar in molecular weight, carbohydrate content and pH optimum.
- Taxon
- Peanut
Arachis hypogaeat0 - Outcome
- MW, carbohydrate content and pH optimume1
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Comparative Study Of The Isozymes Of The Cationic And The Anionic Peanut Peroxidases”
e1“They are similar in MW, carbohydrate content and pH optimum for catalysis”
Claim · model-written summary
The cationic and anionic peanut peroxidases differ in isoelectric point.
- Taxon
- PeanutArachis hypogaeat0
- Outcome
- isoelectric pointe2
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Comparative Study Of The Isozymes Of The Cationic And The Anionic Peanut Peroxidases”
e2“contents and isoelectric point”
Claim · model-written summary
The cationic and anionic peanut peroxidases differ in Ca content.
- Taxon
- PeanutArachis hypogaeat0
- Outcome
- Cae3
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Comparative Study Of The Isozymes Of The Cationic And The Anionic Peanut Peroxidases”
e3“but differ in Ca”
Claim · model-written summary
The cationic peroxidase C.PRX is released into the medium about four times as much as the anionic A.PRX.
- Taxon
- PeanutArachis hypogaeat0
- Gene
- C.PRXe5
- Outcome
- released into the mediume5
- Value
- four times as muche5
- Comparator
- A.PRXe5
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Comparative Study Of The Isozymes Of The Cationic And The Anionic Peanut Peroxidases”
e5“four times as much C.PRX is released into the medium as the A.PRX”
Claim · model-written summary
C.PRX and A.PRX do not differ substantially in their rate of synthesis.
- Taxon
- PeanutArachis hypogaeat0
- Outcome
- rate of their synthesise6
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Comparative Study Of The Isozymes Of The Cationic And The Anionic Peanut Peroxidases”
e6“no substantial difference was observed in the rate of their synthesis”
Claim · model-written summary
Tunicamycin, an inhibitor of N-linked glycosylation, did not prevent release of the peroxidases into the medium.
- Taxon
- PeanutArachis hypogaeat0
- Treatment
- treatment of the cultures with tunicamycine7
- Outcome
- releasee7
- Direction
- not preventede7
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Comparative Study Of The Isozymes Of The Cationic And The Anionic Peanut Peroxidases”
e7“This release is not prevented by treatment of the cultures with tunicamycin, an inhibitor of N-linked glycosylation”
Claim · model-written summary
Both peroxidases are associated with Golgi complexes and amyloplasts.
- Taxon
- PeanutArachis hypogaeat0
- Organ / stage
- Golgi complexes and amyloplastse1
- Outcome
- associated withe1
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Comparative Study Of The Isozymes Of The Cationic And The Anionic Peanut Peroxidases”
e1“both peroxidases are associated with Golgi complexes and amyloplasts”
Claim · model-written summary
The cationic peroxidase C.PRX is found on the cell walls.
- Taxon
- PeanutArachis hypogaeat0
- Organ / stage
- cell wallse2
- Gene
- C.PRXe2
- Outcome
- founde2
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Comparative Study Of The Isozymes Of The Cationic And The Anionic Peanut Peroxidases”
e2“The C.PRX is also found on the cell walls”
Claim · model-written summary
The anionic peroxidase A.PRX is found on the plasmalemma.
- Taxon
- PeanutArachis hypogaeat0
- Organ / stage
- plasmalemmae3
- Gene
- A.PRXe3
- Outcome
- on the plasmalemmae3
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Comparative Study Of The Isozymes Of The Cationic And The Anionic Peanut Peroxidases”
e3“while the A.PRX on the plasmalemma”
Claim · model-written summary
Carbohydrate side chains on the peroxidase surface are essential for expression of enzyme activity, according to the authors.
- Taxon
- PeanutArachis hypogaeat0
- Outcome
- expression of the enzyme activitye4
- Qualifier
- carbohydrate side chains distributed on the surface of the peroxidasese4
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Comparative Study Of The Isozymes Of The Cationic And The Anionic Peanut Peroxidases”
e4“carbohydrate side chains distributed on the surface of the peroxidases are essential for expression of the enzyme activity”
Claim · model-written summary
Carbohydrate side chains on the peroxidase surface are essential for maintenance of molecular stability, according to the authors.
- Taxon
- PeanutArachis hypogaeat0
- Outcome
- maintenance of the stability of the moleculese5
- Qualifier
- carbohydrate side chains distributed on the surface of the peroxidasese4
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Comparative Study Of The Isozymes Of The Cationic And The Anionic Peanut Peroxidases”
e4“carbohydrate side chains distributed on the surface of the peroxidases are essential for expression of the enzyme activity and for maintenance of the stability of the molecules”
e5“for maintenance of the stability of the molecules”
Claim · model-written summary
The isoelectric point difference between the two isozymes is attributed to their relative content of acidic and basic amino acids.
- Taxon
- PeanutArachis hypogaeat0
- Outcome
- difference in pIe4
- Qualifier
- different relative content of the acidic and basic amino acidse4
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Comparative Study Of The Isozymes Of The Cationic And The Anionic Peanut Peroxidases”
e4“The basis for the difference in pI is found in the different relative content of the acidic and basic amino acids”
Claim · model-written summary
Polyclonal antisera to each isozyme reacted with both the homologous and the non-homologous isozyme.
- Taxon
- PeanutArachis hypogaeat0
- Outcome
- reactede6
- Qualifier
- non-homologous isozymee6
- Comparator
- homologouse6
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Comparative Study Of The Isozymes Of The Cationic And The Anionic Peanut Peroxidases”
e6“The polyclonal antisera reacted not only with the homologous but also with the non-homologous isozyme”
Claim · model-written summary
Monoclonal antibodies recognized the cationic peroxidase C.PRX more specifically.
- Taxon
- PeanutArachis hypogaeat0
- Gene
- C.PRXe7
- Outcome
- recognized more specificallye7
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Comparative Study Of The Isozymes Of The Cationic And The Anionic Peanut Peroxidases”
e7“the monoclonal antibodies recognized more specifically the C.PRX”
Claim · model-written summary
The cross-reaction between the isozymes is partly attributed to epitopes in carbohydrate moieties and near the active sites, according to the authors.
- Taxon
- PeanutArachis hypogaeat0
- Outcome
- cross-reactione0
- Qualifier
- epitopes present in the carbohydrate moieties and near the active sites of the isozymese0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Comparative Study Of The Isozymes Of The Cationic And The Anionic Peanut Peroxidases”
e0“The cross-reaction is partially attributed to the epitopes present in the carbohydrate moieties and near the active sites of the isozymes”